1Q35

Crystal Structure of Pasteurella haemolytica Apo Ferric ion-Binding Protein A

1Q35 の概要

• エントリーDOI: 10.2210/pdb1q35/pdb
• 分子名称: iron binding protein FbpA, 1,2-ETHANEDIOL, FORMIC ACID, ... (4 entities in total)
• 機能のキーワード: iron binding protein, metal binding protein
• 由来する生物種: Mannheimia haemolytica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36048.92

構造登録者

Shouldice, S.R.,Dougan, D.R.,Skene, R.J.,Snell, G.,Scheibe, D.,Williams, P.A.,Kirby, S.,McRee, D.E.,Schryvers, A.B.,Tari, L.W. (登録日: 2003-07-28, 公開日: 2003-11-11, 最終更新日: 2024-11-13)

主引用文献

Shouldice, S.R.,Dougan, D.R.,Williams, P.A.,Skene, R.J.,Snell, G.,Scheibe, D.,Kirby, S.,Hosfield, D.J.,McRee, D.E.,Schryvers, A.B.,Tari, L.W.
Crystal structure of Pasteurella haemolytica ferric ion-binding protein A reveals a novel class of bacterial iron-binding proteins
J.Biol.Chem., 278:41093-41098, 2003

PubMed Abstract: Pasteurellosis caused by the Gram-negative pathogen Pasteurella haemolytica is a serious disease leading to death in cattle. To scavenge growth-limiting iron from the host, the pathogen utilizes the periplasmic ferric ion-binding protein A (PhFbpA) as a component of an ATP-binding cassette transport pathway. We report the 1.2-A structure of the iron-free (apo) form of PhFbpA, which is a member of the transferrin structural superfamily. The protein structure adopts a closed conformation, allowing us to reliably assign putative iron-coordinating residues. Based on our analysis, PhFbpA utilizes a unique constellation of binding site residues and anions to octahedrally coordinate an iron atom. A surprising finding in the structure is the presence of two formate anions on opposite sides of the iron-binding pocket. The formate ions tether the N- and C-terminal domains of the protein and stabilize the closed structure, also providing clues as to probable candidates for synergistic anions in the iron-loaded state. PhFbpA represents a new class of bacterial iron-binding proteins.

PubMed: 12882966
DOI: 10.1074/jbc.M306821200

実験手法

X-RAY DIFFRACTION (1.2 Å)